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Results for “GOLGI APPARATUS”

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PubMed1983

The bioenergetics of Golgi apparatus function: evidence for an ATP-dependent proton pump.

The energy requirement for the processing of newly-synthesized proteins by the Golgi was examined. Rat liver Golgi preparations enriched more than 100-fold have high ATPase activity that co-purified with the Golgi marker enzyme galactosyl transferase. The ATPase activity was 80% inhibited by dicyclohexylcarbodiimide and may represent a proton pump. Evidence is presented for a functional role of the ATPase in Golgi. First, measurement of [14C]methylamine uptake demonstrated ATP-dependent acidification. Second, inhibition of the ATPase with dicyclohexylcarbodiimide resulted in a 3-fold accumulation of newly-synthesized protein in the Golgi.

Adenosine Triphosphatases↗
PubMed1993

Overlapping distribution of two glycosyltransferases in the Golgi apparatus of HeLa cells.

Thin, frozen sections of a HeLa cell line were double labeled with specific antibodies to localize the trans-Golgi enzyme, beta 1,4 galactosyltransferase (GalT) and the medial enzyme, N-acetylglucosaminyltransferase I (NAGT I). The latter was detected by generating a HeLa cell line stably expressing a myc-tagged version of the endogenous protein. GalT was found in the trans-cisterna and trans-Golgi network but, contrary to expectation, NAGT I was found both in the medial- and trans-cisternae, overlapping the distribution of GalT. About one third of the NAGT I and half of the GalT were found in the shared, trans-cisterna. These data show that the differences between cisternae are determined not by different sets of enzymes but by different mixtures.

Base Sequence↗